Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors

Schaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L (1998)
FEBS LETTERS 421(1): 80-82.

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Schaschke N, Assfalg-Machleidt I, Machleidt W, Moroder L. Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS. 1998;421(1):80-82.
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., & Moroder, L. (1998). Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS, 421(1), 80-82. doi:10.1016/S0014-5793(97)01538-X
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., and Moroder, L. (1998). Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS 421, 80-82.
Schaschke, N., et al., 1998. Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS, 421(1), p 80-82.
N. Schaschke, et al., “Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors”, FEBS LETTERS, vol. 421, 1998, pp. 80-82.
Schaschke, N., Assfalg-Machleidt, I., Machleidt, W., Moroder, L.: Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors. FEBS LETTERS. 421, 80-82 (1998).
Schaschke, Norbert, Assfalg-Machleidt, I, Machleidt, W, and Moroder, L. “Substrate/propeptide-derived endo-epoxysuccinyl peptides as highly potent and selective cathepsin B inhibitors”. FEBS LETTERS 421.1 (1998): 80-82.
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17 Citations in Europe PMC

Data provided by Europe PubMed Central.

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Dana D, Davalos AR, De S, Rathod P, Gamage RK, Huestis J, Afzal N, Zavlanov Y, Paroly SS, Rotenberg SA, Subramaniam G, Mark KJ, Chang EJ, Kumar S., Bioorg Med Chem 21(11), 2013
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Design, synthesis, and evaluation of in vivo potency and selectivity of epoxysuccinyl-based inhibitors of papain-family cysteine proteases.
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Cathepsin B is essential for regeneration of scratch-wounded normal human epidermal keratinocytes.
Büth H, Luigi Buttigieg P, Ostafe R, Rehders M, Dannenmann SR, Schaschke N, Stark HJ, Boukamp P, Brix K., Eur J Cell Biol 86(11-12), 2007
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Epoxysuccinyl peptide-derived cathepsin B inhibitors: modulating membrane permeability by conjugation with the C-terminal heptapeptide segment of penetratin.
Schaschke N, Deluca D, Assfalg-Machleidt I, Höhneke C, Sommerhoff CP, Machleidt W., Biol Chem 383(5), 2002
PMID: 12108551
Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation.
Balaji KN, Schaschke N, Machleidt W, Catalfamo M, Henkart PA., J Exp Med 196(4), 2002
PMID: 12186841
Crystal structure of cathepsin X: a flip-flop of the ring of His23 allows carboxy-monopeptidase and carboxy-dipeptidase activity of the protease.
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PMID: 10745011
Beta-cyclodextrin/epoxysuccinyl peptide conjugates: a new drug targeting system for tumor cells.
Schaschke N, Assfalg-Machleidt I, Machleidt W, Lassleben T, Sommerhoff CP, Moroder L., Bioorg Med Chem Lett 10(7), 2000
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Highly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections.
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Epoxysuccinyl peptide-derived affinity labels for cathepsin B.
Schaschke N, Assfalg-Machleidt I, Lassleben T, Sommerhoff CP, Moroder L, Machleidt W., FEBS Lett 482(1-2), 2000
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Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?
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